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LL-37 (Human Cathelicidin Antimicrobial Peptide)
Also known as: Cathelicidin, hCAP-18, CAMP
Confidence
Updated 2026-03-18
LL-37 is the only human cathelicidin antimicrobial peptide, a 37-amino acid peptide cleaved from the precursor protein hCAP-18. It serves as a critical component of innate immunity with broad-spectrum antimicrobial activity against bacteria, fungi, and enveloped viruses. Beyond direct antimicrobial action, it modulates inflammation, wound healing, and immune cell recruitment.
Class
Antimicrobial Peptide
Routes
Subcutaneous, Topical, Intravenous (research)
Half-Life
Not well established. Rapidly degraded by proteases in serum (~30 minutes in vitro). Tissue persistence may be longer.
LL-37 disrupts microbial membranes through electrostatic interaction with negatively charged lipid bilayers, forming pores that cause cell lysis. Additionally, it neutralizes lipopolysaccharide (LPS/endotoxin), recruits immune cells via formyl peptide receptor-like 1 (FPRL1), stimulates angiogenesis, promotes wound healing through keratinocyte and fibroblast migration, and modulates dendritic cell and macrophage function.
Half-Life
Not well established. Rapidly degraded by proteases in serum (~30 minutes in vitro). Tissue persistence may be longer.
Bioavailability
Not established for systemic administration. Primarily studied for local/topical application.
No approved indications. Research: chronic infections (biofilm-associated), wound healing, Lyme disease (anecdotal), immune modulation, antimicrobial resistance.
Well-characterized endogenous peptide with extensive basic science literature (thousands of publications). Demonstrated broad-spectrum antimicrobial activity in vitro and in animal models. Clinical evidence is limited to small studies and case reports. Popular in integrative/functional medicine for chronic infection support, particularly Lyme disease — but clinical evidence for this use is largely anecdotal.
Human Studies
8
Animal Studies
100
Endogenous peptide, so theoretically well-tolerated. At high concentrations, LL-37 can be cytotoxic to host cells. May trigger mast cell degranulation. Overexpression implicated in psoriasis and rosacea pathogenesis. Injection site reactions. Systemic administration safety poorly characterized.
Investigational. Sold as a research peptide. Used off-label in some integrative medicine practices. Several pharmaceutical companies developing synthetic analogs for topical antimicrobial applications.
Drug Interactions: Theoretical interactions with immunosuppressants. May be degraded by protease-rich environments. Monitoring: Infection markers, wound healing progression, immune cell panels. Research Gaps: Optimal route, dose, and duration for therapeutic use unknown. Systemic PK not characterized. Role in chronic Lyme is not evidence-based.
Subcutaneous (research context)
Common Range
50–200 mcg (typical research doses)
Timing
Variable
Frequency
Daily to twice weekly (no established protocol)
Cycling
Not established
Reconstitution
Reconstitute lyophilized powder with bacteriostatic water
Storage
Refrigerated after reconstitution
Important Note
NOT FDA-approved. Primarily supported by in vitro and animal data. Clinical protocols are empirical and not validated. Research context only.
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Immune Modulator
Thymosin alpha-1 is a 28-amino acid peptide originally isolated from thymic tissue. It is approved in over 35 countries (not the US) under the brand name Zadaxin for immune modulation in hepatitis B and as an adjunct to chemotherapy. It represents a unique case in peptide regulation — internationally validated but caught in US regulatory limbo.
Anti-Inflammatory Peptide
KPV is a naturally occurring tripeptide derived from the C-terminal end of alpha-melanocyte-stimulating hormone (alpha-MSH). It retains the potent anti-inflammatory properties of the parent hormone without melanocortin receptor activation (no tanning or hormonal effects). It has gained significant interest in functional medicine for gut inflammation, particularly inflammatory bowel disease.
Tissue Repair & Regeneration
BPC-157 is a synthetic pentadecapeptide derived from a protective protein found in human gastric juice. It has generated extraordinary interest for its broad cytoprotective and regenerative effects observed in preclinical studies across virtually every organ system studied. Despite this promise, it remains one of the most controversial peptides due to the near-complete absence of human clinical trial data.
Disclaimer: This content is for educational and informational purposes only and does not constitute medical advice. Always consult with a licensed healthcare provider before starting, stopping, or modifying any peptide therapy. PeptideSupplierMatch does not prescribe, sell, or distribute peptides.
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